Salsman Jayme, Top Deniz, Boutilier Julie, Duncan Roy
Department of Microbiology and Immunology, Faculty of Medicine, Dalhousie University, Halifax, Nova Scotia B3H 4H7, Canada.
J Virol. 2005 Jul;79(13):8090-100. doi: 10.1128/JVI.79.13.8090-8100.2005.
The fusion-associated small transmembrane (FAST) proteins of the fusogenic reoviruses are the only known examples of membrane fusion proteins encoded by non-enveloped viruses. While the involvement of the FAST proteins in mediating extensive syncytium formation in virus-infected and -transfected cells is well established, the nature of the fusion reaction and the role of cell-cell fusion in the virus replication cycle remain unclear. To address these issues, we analyzed the syncytial phenotype induced by four different FAST proteins: the avian and Nelson Bay reovirus p10, reptilian reovirus p14, and baboon reovirus p15 FAST proteins. Results indicate that FAST protein-mediated cell-cell fusion is a relatively non-leaky process, as demonstrated by the absence of significant [3H]uridine release from cells undergoing fusion and by the resistance of these cells to treatment with hygromycin B, a membrane-impermeable translation inhibitor. However, diminished membrane integrity occurred subsequent to extensive syncytium formation and was associated with DNA fragmentation and chromatin condensation, indicating that extensive cell-cell fusion activates apoptotic signaling cascades. Inhibiting effector caspase activation or ablating the extent of syncytium formation, either by partial deletion of the avian reovirus p10 ecto-domain or by antibody inhibition of p14-mediated cell-cell fusion, all resulted in reduced membrane permeability changes. These observations suggest that the FAST proteins do not possess intrinsic membrane-lytic activity. Rather, extensive FAST protein-induced syncytium formation triggers an apoptotic response that contributes to altered membrane integrity. We propose that the FAST proteins have evolved to serve a dual role in the replication cycle of these fusogenic non-enveloped viruses, with non-leaky cell-cell fusion initially promoting localized cell-cell transmission of the infection followed by enhanced progeny virus release from apoptotic syncytia and systemic dissemination of the infection.
融合性呼肠孤病毒的融合相关小跨膜(FAST)蛋白是无包膜病毒编码的膜融合蛋白的唯一已知实例。虽然FAST蛋白在介导病毒感染和转染细胞中广泛的合胞体形成中的作用已得到充分证实,但融合反应的本质以及细胞间融合在病毒复制周期中的作用仍不清楚。为了解决这些问题,我们分析了四种不同FAST蛋白诱导的合胞体表型:禽呼肠孤病毒和纳尔逊湾呼肠孤病毒的p10蛋白、爬行类呼肠孤病毒的p14蛋白以及狒狒呼肠孤病毒的p15 FAST蛋白。结果表明,FAST蛋白介导的细胞间融合是一个相对非渗漏的过程,这体现在融合细胞中没有显著的[3H]尿苷释放,以及这些细胞对潮霉素B(一种膜不透性翻译抑制剂)处理具有抗性。然而,在广泛的合胞体形成之后,膜完整性会降低,并且与DNA片段化和染色质浓缩相关,这表明广泛的细胞间融合激活了凋亡信号级联反应。通过部分缺失禽呼肠孤病毒p10胞外结构域或通过抗体抑制p14介导的细胞间融合来抑制效应半胱天冬酶激活或减少合胞体形成的程度,均导致膜通透性变化降低。这些观察结果表明,FAST蛋白不具有内在的膜溶解活性。相反,广泛的FAST蛋白诱导的合胞体形成触发了一种凋亡反应,这导致膜完整性改变。我们提出,FAST蛋白在这些融合性无包膜病毒的复制周期中已进化为发挥双重作用,非渗漏的细胞间融合最初促进感染的局部细胞间传播,随后增强子代病毒从凋亡合胞体中的释放以及感染的全身传播。